OCRL

Oculocerebrorenal syndrome of Lowe
PDB rendering based on 2qv2.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2KIE​, 2QV2​, 3QBT​, 3QIS​, 4CMN​
Identifiers
Symbols	OCRL ; INPP5F; LOCR; NPHL2; OCRL-1; OCRL1
External IDs	OMIM: 300535 MGI: 109589 HomoloGene: 233 IUPHAR: 1460 GeneCards: OCRL Gene
EC number	3.1.3.36
Gene ontology Molecular function • phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity • GTPase activator activity • protein binding • Rac GTPase binding • inositol phosphate phosphatase activity Cellular component • photoreceptor outer segment • nucleus • cytoplasm • early endosome • Golgi stack • Golgi-associated vesicle • trans-Golgi network • cytosol • plasma membrane • coated pit • clathrin-coated vesicle • phagocytic vesicle membrane • early endosome membrane • extracellular exosome Biological process • in utero embryonic development • protein dephosphorylation • lipid metabolic process • phospholipid metabolic process • phosphatidylinositol biosynthetic process • small GTPase mediated signal transduction • cilium assembly • regulation of GTPase activity • positive regulation of GTPase activity • inositol phosphate metabolic process • small molecule metabolic process • phosphatidylinositol dephosphorylation • regulation of small GTPase mediated signal transduction Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4952	320634
Ensembl	ENSG00000122126	ENSMUSG00000001173
UniProt	Q01968	Q6NVF0
RefSeq (mRNA)	NM_000276	NM_177215
RefSeq (protein)	NP_000267	NP_796189
Location (UCSC)	Chr X: 129.54 – 129.59 Mb	Chr X: 47.91 – 47.97 Mb
PubMed search

Inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F), also known as Lowe oculocerebrorenal syndrome protein, is an enzyme encoded by the OCRL gene located on the X chromosome in humans.^[1]

This gene encodes a phosphatase enzyme involved in actin polymerization, and is found in the trans-Golgi network.^[1]

Mutation in this gene are associated with oculocerebrorenal syndrome^[2] and also with Dent's disease.^[3][4]

References

1. "Entrez Gene: oculocerebrorenal syndrome of Lowe".
2. Kawano T, Indo Y, Nakazato H, Shimadzu M, Matsuda I (June 1998). "Oculocerebrorenal syndrome of Lowe: three mutations in the OCRL1 gene derived from three patients with different phenotypes". Am. J. Med. Genet. 77 (5): 348–55. doi:10.1002/(SICI)1096-8628(19980605)77:5<348::AID-AJMG2>3.0.CO;2-J. PMID 9632163.
3. Online 'Mendelian Inheritance in Man' (OMIM) 300555
4. Hoopes RR, Shrimpton AE, Knohl SJ, et al. (February 2005). "Dent Disease with mutations in OCRL1". Am. J. Hum. Genet. 76 (2): 260–7. doi:10.1086/427887. PMC 1196371. PMID 15627218.

Further reading

• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome.". Nature 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
• Erdmann KS, Mao Y, McCrea HJ, et al. (2007). "A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway.". Dev. Cell 13 (3): 377–90. doi:10.1016/j.devcel.2007.08.004. PMC 2025683. PMID 17765681.
• Hyvola N, Diao A, McKenzie E, et al. (2006). "Membrane targeting and activation of the Lowe syndrome protein OCRL1 by rab GTPases.". EMBO J. 25 (16): 3750–61. doi:10.1038/sj.emboj.7601274. PMC 1553191. PMID 16902405.
• Mao Y, Balkin DM, Zoncu R, et al. (2009). "A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism.". EMBO J. 28 (13): 1831–42. doi:10.1038/emboj.2009.155. PMC 2711190. PMID 19536138.
• Suchy SF, Cronin JC, Nussbaum RL (2009). "Abnormal bradykinin signalling in fibroblasts deficient in the PIP(2) 5-phosphatase, ocrl1.". J. Inherit. Metab. Dis. 32 (2): 280–8. doi:10.1007/s10545-009-1058-3. PMID 19172411.
• Wu F, Reed AA, Williams SE, et al. (2009). "Mutational analysis of CLC-5, cofilin and CLC-4 in patients with Dent's disease.". Nephron Physiol 112 (4): 53–62. doi:10.1159/000225944. PMID 19546591.
• Coon BG, Mukherjee D, Hanna CB, et al. (2009). "Lowe syndrome patient fibroblasts display Ocrl1-specific cell migration defects that cannot be rescued by the homologous Inpp5b phosphatase.". Hum. Mol. Genet. 18 (23): 4478–91. doi:10.1093/hmg/ddp407. PMID 19700499.
• Tosetto E, Addis M, Caridi G, et al. (2009). "Locus heterogeneity of Dent's disease: OCRL1 and TMEM27 genes in patients with no CLCN5 mutations.". Pediatr. Nephrol. 24 (10): 1967–73. doi:10.1007/s00467-009-1228-4. PMID 19582483.
• Faucherre A, Desbois P, Nagano F, et al. (2005). "Lowe syndrome protein Ocrl1 is translocated to membrane ruffles upon Rac GTPase activation: a new perspective on Lowe syndrome pathophysiology.". Hum. Mol. Genet. 14 (11): 1441–8. doi:10.1093/hmg/ddi153. PMID 15829501.
• Shrimpton AE, Hoopes RR, Knohl SJ, et al. (2009). "OCRL1 mutations in Dent 2 patients suggest a mechanism for phenotypic variability.". Nephron Physiol 112 (2): 27–36. doi:10.1159/000213506. PMID 19390221.
• Sekine T, Nozu K, Iyengar R, et al. (2007). "OCRL1 mutations in patients with Dent disease phenotype in Japan.". Pediatr. Nephrol. 22 (7): 975–80. doi:10.1007/s00467-007-0454-x. PMID 17384968.
• Chabaâ L, Monnier N, Dahri S; et al. (2006). "[Oculo-cerebro-renal Lowe syndrome: clinical, biochemical and molecular studies in a Moroccan patient]". Ann. Biol. Clin. (Paris) 64 (1): 53–9. PMID 16420990.
• Choudhury R, Diao A, Zhang F, et al. (2005). "Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network.". Mol. Biol. Cell 16 (8): 3467–79. doi:10.1091/mbc.E05-02-0120. PMC 1182289. PMID 15917292.
• Sethi SK, Bagga A, Gulati A, et al. (2008). "Mutations in OCRL1 gene in Indian children with Lowe syndrome.". Clin. Exp. Nephrol. 12 (5): 358–62. doi:10.1007/s10157-008-0059-0. PMID 18500547.
• Cui S, Guerriero CJ, Szalinski CM, et al. (2010). "OCRL1 function in renal epithelial membrane traffic.". Am. J. Physiol. Renal Physiol. 298 (2): F335–45. doi:10.1152/ajprenal.00453.2009. PMC 2822509. PMID 19940034.
• McCrea HJ, Paradise S, Tomasini L, et al. (2008). "All known patient mutations in the ASH-RhoGAP domains of OCRL affect targeting and APPL1 binding.". Biochem. Biophys. Res. Commun. 369 (2): 493–9. doi:10.1016/j.bbrc.2008.02.067. PMC 2442618. PMID 18307981.
• Hoopes RR, Shrimpton AE, Knohl SJ, et al. (2005). "Dent Disease with mutations in OCRL1.". Am. J. Hum. Genet. 76 (2): 260–7. doi:10.1086/427887. PMC 1196371. PMID 15627218.
• Levtchenko EN, Monnens LA, Bökenkamp A, Knoers NV (2007). "[From gene to disease; Dent's disease caused by abnormalities in the CLCN5 and OCRL1 genes]". Ned Tijdschr Geneeskd 151 (43): 2377–80. PMID 18019214.
• Choudhury R, Noakes CJ, McKenzie E, et al. (2009). "Differential clathrin binding and subcellular localization of OCRL1 splice isoforms.". J. Biol. Chem. 284 (15): 9965–73. doi:10.1074/jbc.M807442200. PMC 2665120. PMID 19211563.
• Swan LE, Tomasini L, Pirruccello M, et al. (2010). "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1.". Proc. Natl. Acad. Sci. U.S.A. 107 (8): 3511–6. doi:10.1073/pnas.0914658107. PMC 2840420. PMID 20133602.

External links

• GeneReviews/NCBI/NIH/UW entry on Lowe Syndrome
• OCRL protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)